6OVH

Cryo-EM structure of Bimetallic dodecameric cage design 3 (BMC3) from cytochrome cb562

Summary for 6OVH

• Entry DOI: 10.2210/pdb6ovh/pdb
• EMDB information: 20212
• Descriptor: Soluble cytochrome b562, HEME C, ACETOHYDROXAMIC ACID, ... (6 entities in total)
• Functional Keywords: supramolecular assembly, protein cage, bimetallic, metal binding, hydroxamic acid, metal binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 12
• Total formula weight: 152951.90

Authors

Golub, E.,Subramanian, R.H.,Yan, X.,Alberstein, R.G.,Tezcan, F.A. (deposition date: 2019-05-07, release date: 2020-01-29, Last modification date: 2024-10-23)

Primary citation

Golub, E.,Subramanian, R.H.,Esselborn, J.,Alberstein, R.G.,Bailey, J.B.,Chiong, J.A.,Yan, X.,Booth, T.,Baker, T.S.,Tezcan, F.A.
Constructing protein polyhedra via orthogonal chemical interactions.
Nature, 578:172-176, 2020

PubMed Abstract: Many proteins exist naturally as symmetrical homooligomers or homopolymers. The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design. As synthesized by ribosomes, proteins are inherently asymmetric. Thus, they must acquire multiple surface patches that selectively associate to generate the different symmetry elements needed to form higher-order architectures-a daunting task for protein design. Here we address this problem using an inorganic chemical approach, whereby multiple modes of protein-protein interactions and symmetry are simultaneously achieved by selective, 'one-pot' coordination of soft and hard metal ions. We show that a monomeric protein (protomer) appropriately modified with biologically inspired hydroxamate groups and zinc-binding motifs assembles through concurrent Fe and Zn coordination into discrete dodecameric and hexameric cages. Our cages closely resemble natural polyhedral protein architectures and are, to our knowledge, unique among designed systems in that they possess tightly packed shells devoid of large apertures. At the same time, they can assemble and disassemble in response to diverse stimuli, owing to their heterobimetallic construction on minimal interprotein-bonding footprints. With stoichiometries ranging from [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein cages represent some of the compositionally most complex protein assemblies-or inorganic coordination complexes-obtained by design.

PubMed: 31969701
DOI: 10.1038/s41586-019-1928-2

Experimental method

ELECTRON MICROSCOPY (2.6 Å)